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肿瘤坏死因子受体死亡结构域相关蛋白TRADD和FADD发出酸性鞘磷脂酶激活的信号。

TNF receptor death domain-associated proteins TRADD and FADD signal activation of acid sphingomyelinase.

作者信息

Schwandner R, Wiegmann K, Bernardo K, Kreder D, Kronke M

机构信息

Institute of Immunology, Christian-Albrechts University of Kiel, Brunswiker Strasse 4, 24105 Kiel, Germany.

出版信息

J Biol Chem. 1998 Mar 6;273(10):5916-22. doi: 10.1074/jbc.273.10.5916.

Abstract

Sphingomyelinase (SMase) activation and ceramide generation have emerged as an important signaling pathway transducing diverse biological effects of cytokine receptors like p55 tumor necrosis factor (TNF) receptor or Fas. Here we describe the TNF-dependent activation of acid SMase (A-SMase) through the p55 TNF receptor-associated proteins TRADD and FADD. Overexpression of TRADD and FADD in 293 cells did not change basal activity of A-SMase but enhanced TNF-induced stimulation of A-SMase. Other TNF R55-associated proteins like TRAF2 and RIP, which were reported to mediate TNF R55-mediated activation of nuclear factor kappaB, did not affect activation of A-SMase. Caspase inhibitors markedly reduced A-SMase activity, suggesting the involvement of an ICE-like protease in TRADD/FADD-mediated activation of A-SMase. Overexpression of caspase-8/a (FLICE/MACH) or caspase-10/b (FLICE2) did not change A-SMase activity, suggesting that TRADD/FADD-mediated activation of A-SMase involves a yet to be defined caspase-like protease distinct from caspase-8/a or -10/b.

摘要

鞘磷脂酶(SMase)激活和神经酰胺生成已成为转导细胞因子受体(如p55肿瘤坏死因子(TNF)受体或Fas)多种生物学效应的重要信号通路。在此我们描述了通过p55 TNF受体相关蛋白TRADD和FADD对酸性SMase(A-SMase)的TNF依赖性激活。在293细胞中过表达TRADD和FADD不会改变A-SMase的基础活性,但会增强TNF诱导的A-SMase刺激。其他TNF R55相关蛋白,如据报道介导TNF R55介导的核因子κB激活的TRAF2和RIP,不会影响A-SMase的激活。半胱天冬酶抑制剂显著降低A-SMase活性,提示一种类ICE蛋白酶参与TRADD/FADD介导的A-SMase激活。过表达半胱天冬酶-8/a(FLICE/MACH)或半胱天冬酶-10/b(FLICE2)不会改变A-SMase活性,提示TRADD/FADD介导的A-SMase激活涉及一种不同于半胱天冬酶-8/a或-10/b的尚未明确的类半胱天冬酶蛋白酶。

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